title: The effects of Bacillus thuringiensis Cry6A on the survival, growth, reproduction, locomotion, and behavioral response of Caenorhabditis elegans.
abstract: Several families of crystal proteins from Bacillus thuringiensis exhibit nematicidal activity. Cry5B protein, a pore-forming toxin, has been intensively studied yielding many insights into the mode of action of crystal protein at molecular level and pathogenesis of pore-forming toxins. However, little attention was paid to Cry6A, another representative nematicidal crystal protein. Cry6A shares very low homology with Cry5B at amino acid sequence and probably acts in a distinct pathway from Cry5B and even the other main commercial crystal proteins. In the current study, we comprehensively investigated the nematicidal properties of Cry6Aa2 against the free-living soil nematode Caenorhabditis elegans and examined the physical response of C. elegans to Cry6Aa2 attack. Our results indicate that Cry6Aa2 exhibits high lethal activity to C. elegans and could cause detrimental effects on C. elegans, including obviously suppressed growth, decreased brood size, and even abnormal motility. Meanwhile, our study additionally shows that C. elegans could defend against the Cry6Aa2 toxin harmful threat through behavioral defense responses, such as reduced oral uptake and physical avoidance. In general, this study suggests that Cry6Aa2 possesses diverse nematicidal properties, which strongly indicates that Cry6Aa2 is a promising potential candidate of nematicidal agent. Moreover, this study highlights the importance of behavioral responses in defense of C. elegans for survival and demonstrates the key role of crystal protein in the interaction of B. thuringiensis-C. elegans. These findings could shed light on understanding the interaction of C. elegans with B. thuringiensis and provide a perfect model to study the role of pathogenic factor in the interaction of pathogen-host.
authors.affiliation: State Key Laboratory of Breeding Base of Microbial Molecular Biology, College of Life Science, Hunan Normal University, Changsha, 410081, People's Republic of China.
authors.forename: Hui
authors.initials: H
authors.lastname: Luo
authors.forename: Jing
authors.initials: J
authors.lastname: Xiong
authors.forename: Qiaoni
authors.initials: Q
authors.lastname: Zhou
authors.forename: Liqiu
authors.initials: L
authors.lastname: Xia
authors.forename: Ziquan
authors.initials: Z
authors.lastname: Yu
mesh_terms: D000818:Animals; D000969:Antinematodal Agents / Q000494:pharmacology*; D001413:Bacillus thuringiensis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism / Q000494:pharmacology*; D017173:Caenorhabditis elegans / Q000187:drug effects* / Q000254:growth & development / Q000502:physiology*; D002470:Cell Survival / Q000187:drug effects; D004731:Endotoxins / Q000378:metabolism / Q000494:pharmacology*; D006460:Hemolysin Proteins / Q000378:metabolism / Q000494:pharmacology*; D012098:Reproduction / Q000187:drug effects
chemical_list: D000969:Antinematodal Agents; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis